Acay, HilalUzan, SerhatBaran, Mehmet FıratBilden, AlicanAygün, Hüsamettin2021-10-302021-10-302020Aygun, H.; Department of Biology, Faculty of Science, Dicle University, Diyarbakir, Turkey.https://www.scopus.com/record/display.uri?eid=2-s2.0-85086788493&doi=10.1007%2fs00764-020-00030-3&origin=inward&txGid=0832669ef3d3615f6e45fcd42d07387b&featureToggles=FEATURE_VIEW_PDF:1https://hdl.handle.net/20.500.12514/2917It is known that textile dyes have various risks on human health. Glutathione-S-transferase enzymes play a critical role in the detoxification of xenobiotics in living systems. This study aimed to examine the interaction of methylene blue with human erythrocyte glutathione-S-transferase purified in one step. Human erythrocyte glutathione-S-transferase was purified with approximately 750-fold purification and 30% efficiency by glutathione agarose affinity chromatography. The results showed that the enzyme was inhibited by methylene blue with an IC50 value of 1.40 mmol/L. The Ki constant of methylene blue was 1.17 mmol/L. The Lineweaver–Burk graph of the methylene blue showed that the type of inhibition was compatible with mixed type inhibition. A new third spot was also detected by thin-layer chromatography. Furthermore, the cytotoxicity of methylene blue on human erythrocytes was evaluated and it was found that the haemolysis per cent of methylene blue on erythrocytes was approximately 14%.en10.1007/s00764-020-00030-3info:eu-repo/semantics/openAccessGlutathione-S-transferase . Methylene blue . Thin-layer chromatography . Affinity chromatographyArticle333263269Q4N/AWOS:0005429270000012-s2.0-85086788493